Binding Specificities of Nanobody•Membrane Protein Complexes Obtained from Chemical Cross-Linking and High-Mass MALDI Mass Spectrometry-Reference-Cited by-同舟云学术

Binding Specificities of Nanobody•Membrane Protein Complexes Obtained from Chemical Cross-Linking and High-Mass MALDI Mass Spectrometry

Published:2018-03-21 Issue:8 Volume:90 Page:5306-5313
ISSN:0003-2700
Container-title:Analytical Chemistry
language:en
Short-container-title:Anal. Chem.

Author:

Köhler Martin¹^ORCID,Neff Christoph¹,Perez Camilo²,Brunner Cyrill¹,Pardon Els,Steyaert Jan,Schneider Gisbert¹^ORCID,Locher Kaspar P.²,Zenobi Renato¹^ORCID

Affiliation:

1. Department of Chemistry and Applied Biosciences, ETH Zürich, Vladimir-Prelog-Weg 3, 8093 Zurich, Switzerland

2. Institute of Molecular Biology and Biophysics, ETH Zürich, Otto-Stern-Weg 5, 8093 Zurich, Switzerland

Funder

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung

Publisher

American Chemical Society (ACS)

Subject

Analytical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.analchem.8b00236

Reference44 articles.

1. SbsB structure and lattice reconstruction unveil Ca2+ triggered S-layer assembly

2. Crystal structure of a heterodimer of editosome interaction proteins in complex with two copies of a cross-reacting nanobody

3. Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes

4. Crystal structure of a LacY–nanobody complex in a periplasmic-open conformation

5. Structural basis of inhibition of lipid-linked oligosaccharide flippase PglK by a conformational nanobody

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